BMRB Entry 20103

Name: Structural studies of antimicrobial peptide XT-7 and its Lysine4 analogue
Published: 2010-02-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20103

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structural studies of antimicrobial peptide XT-7 and its Lysine4 analogue

Deposition date:

2009-09-24

Original release date:

2010-02-25

Authors:

Subasinghage, Anusha; Hewage, Chandralal; Conlon, Michael

Citation:

Citation: Subasinghage, Anusha; Conlon, Michael; Hewage, Chandralal. "Development of potent anti-infective agents from Silurana tropicalis: Conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7" Biochim. Biophys. Acta 1804, 1020-1028 (2010).
PubMed: 20116461

Assembly members:

Assembly members:
[Lysine4]XT-7, polymer, 18 residues, Formula weight is not available

Natural source:

Natural source: Common Name: western clawed frog Taxonomy ID: 8364 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Silurana tropicalis

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
[Lysine4]XT-7: GLLKPLLKIAAKVGSNLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	128

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	[Lysine4]XT-7	1

Entities:

Entity 1, [Lysine4]XT-7 18 residues - Formula weight is not available

1

GLY

LEU

LYS

PRO

LEU

LYS

ILE

ALA

2

ALA

LYS

VAL

GLY

SER

ASN

LEU

Samples:

sample_1: [Lysine4]XT-7 2 mM

sample_conditions_1: pH: 3.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
1D	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.11, Goddard - chemical shift assignment, peak picking

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, structure solution

SYBYL v6.8.1, Tripos - refinement

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker DRX 500 MHz